메뉴 건너뛰기




Volumn 579, Issue 1, 2005, Pages 53-58

Requirement of tyrosylprotein sulfotransferase-A for proper cuticle formation in the nematode C. elegans

Author keywords

Caenorhabditis elegans; Collagen; Cuticle formation; Tyrosylprotein sulfotransferase

Indexed keywords

COLLAGEN; SULFOTRANSFERASE;

EID: 11144291215     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.11.044     Document Type: Article
Times cited : (17)

References (32)
  • 1
    • 0019980586 scopus 로고
    • Sulphation of tyrosine residues - A widespread modification of proteins
    • W.B. Huttner Sulphation of tyrosine residues - a widespread modification of proteins Nature 299 1982 273 276
    • (1982) Nature , vol.299 , pp. 273-276
    • Huttner, W.B.1
  • 2
    • 0023851252 scopus 로고
    • Tyrosine sulfation and the secretory pathway
    • W.B. Huttner Tyrosine sulfation and the secretory pathway Annu. Rev. Physiol. 50 1988 363 376
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 363-376
    • Huttner, W.B.1
  • 4
    • 0025361117 scopus 로고
    • Occurrence of tyrosine sulfate in proteins - A balance sheet. 1. Secretory and lysosomal proteins
    • A. Hille, T. Braulke, K. von Figura, and W.B. Huttner Occurrence of tyrosine sulfate in proteins - a balance sheet. 1. Secretory and lysosomal proteins Eur. J. Biochem. 188 1990 577 586
    • (1990) Eur. J. Biochem. , vol.188 , pp. 577-586
    • Hille, A.1    Braulke, T.2    Von Figura, K.3    Huttner, W.B.4
  • 5
    • 0025268088 scopus 로고
    • Occurrence of tyrosine sulfate in proteins - A balance sheet. 2. Membrane proteins
    • A. Hille, and W.B. Huttner Occurrence of tyrosine sulfate in proteins - a balance sheet. 2. Membrane proteins Eur. J. Biochem. 188 1990 587 596
    • (1990) Eur. J. Biochem. , vol.188 , pp. 587-596
    • Hille, A.1    Huttner, W.B.2
  • 6
    • 2542445645 scopus 로고    scopus 로고
    • Zebrafish tyrosylprotein sulfotransferase: Molecular cloning, expression, and functional characterization
    • E. Mishiro, M.Y. Liu, Y. Sakakibara, M. Suiko, and M.C. Liu Zebrafish tyrosylprotein sulfotransferase: molecular cloning, expression, and functional characterization Biochem. Cell Biol. 82 2004 295 303
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 295-303
    • Mishiro, E.1    Liu, M.Y.2    Sakakibara, Y.3    Suiko, M.4    Liu, M.C.5
  • 7
    • 0032530962 scopus 로고    scopus 로고
    • Existence of distinct tyrosylprotein sulfotransferase genes: Molecular characterization of tyrosylprotein sulfotransferase-2
    • R. Beisswanger Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2 Proc. Natl. Acad. Sci. USA 95 1998 11134 11139
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11134-11139
    • Beisswanger, R.1
  • 8
    • 0032544738 scopus 로고    scopus 로고
    • Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans
    • Y.B. Ouyang, and K.L. Moore Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans J. Biol. Chem. 273 1998 24770 24774
    • (1998) J. Biol. Chem. , vol.273 , pp. 24770-24774
    • Ouyang, Y.B.1    Moore, K.L.2
  • 9
    • 0032539889 scopus 로고    scopus 로고
    • Tyrosylprotein sulfotransferase: Purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins
    • Y. Ouyang, W.S. Lane, and K.L. Moore Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins Proc. Natl. Acad. Sci. USA 95 1998 2896 2901
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2896-2901
    • Ouyang, Y.1    Lane, W.S.2    Moore, K.L.3
  • 10
    • 0028309643 scopus 로고
    • 3′-Phosphoadenosine 5′-phosphosulfate biosynthesis and thesulfation of cholecystokinin by the tyrosylprotein-sulfotransferase in rat brain tissue
    • F. Vargas, O. Frerot, F. Brion, M.D. Trung Tuong, A. Lafitte, and C. Gulat-Marnay 3′-Phosphoadenosine 5′-phosphosulfate biosynthesis and thesulfation of cholecystokinin by the tyrosylprotein-sulfotransferase in rat brain tissue Chem. Biol. Interact. 92 1994 281 291
    • (1994) Chem. Biol. Interact. , vol.92 , pp. 281-291
    • Vargas, F.1    Frerot, O.2    Brion, F.3    Trung Tuong, M.D.4    Lafitte, A.5    Gulat-Marnay, C.6
  • 11
    • 0027022996 scopus 로고
    • Post-translational modification of protein by tyrosine sulfation: Active sulfate PAPS is the essential substrate for this modification
    • M. Suiko, P.H. Fernando, Y. Sakakibara, H. Nakajima, M.C. Liu, S. Abe, and S. Nakatsu Post-translational modification of protein by tyrosine sulfation: active sulfate PAPS is the essential substrate for this modification Nucl. Acids Symp. Ser. 1992 183 184
    • (1992) Nucl. Acids Symp. Ser. , pp. 183-184
    • Suiko, M.1    Fernando, P.H.2    Sakakibara, Y.3    Nakajima, H.4    Liu, M.C.5    Abe, S.6    Nakatsu, S.7
  • 12
    • 0037143669 scopus 로고    scopus 로고
    • Tyrosine sulfation of CCR5 N-terminal peptide by tyrosylprotein sulfotransferases 1 and 2 follows a discrete pattern and temporal sequence
    • C. Seibert, M. Cadene, A. Sanfiz, B.T. Chait, and T.P. Sakmar Tyrosine sulfation of CCR5 N-terminal peptide by tyrosylprotein sulfotransferases 1 and 2 follows a discrete pattern and temporal sequence Proc. Natl. Acad. Sci. USA 99 2002 11031 11036
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11031-11036
    • Seibert, C.1    Cadene, M.2    Sanfiz, A.3    Chait, B.T.4    Sakmar, T.P.5
  • 13
    • 0028863479 scopus 로고
    • PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • T. Pouyani, and B. Seed PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus Cell 83 1995 333 343
    • (1995) Cell , vol.83 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 14
    • 0029132217 scopus 로고
    • Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin
    • P.P. Wilkins, K.L. Moore, R.P. McEver, and R.D. Cummings Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin J. Biol. Chem. 270 1995 22677 22680
    • (1995) J. Biol. Chem. , vol.270 , pp. 22677-22680
    • Wilkins, P.P.1    Moore, K.L.2    McEver, R.P.3    Cummings, R.D.4
  • 15
    • 0026565453 scopus 로고
    • A2 domain of human recombinant-derived factor VIII is required for procoagulant activity but not for thrombin cleavage
    • D.D. Pittman, M. Millenson, K. Marquette, K. Bauer, and R.J. Kaufman A2 domain of human recombinant-derived factor VIII is required for procoagulant activity but not for thrombin cleavage Blood 79 1992 389 397
    • (1992) Blood , vol.79 , pp. 389-397
    • Pittman, D.D.1    Millenson, M.2    Marquette, K.3    Bauer, K.4    Kaufman, R.J.5
  • 16
    • 0025924755 scopus 로고
    • Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor
    • A. Leyte, H.B. van Schijndel, C. Niehrs, W.B. Huttner, M.P. Verbeet, K. Mertens, and J.A. van Mourik Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor J. Biol. Chem. 266 1991 740 746
    • (1991) J. Biol. Chem. , vol.266 , pp. 740-746
    • Leyte, A.1    Van Schijndel, H.B.2    Niehrs, C.3    Huttner, W.B.4    Verbeet, M.P.5    Mertens, K.6    Van Mourik, J.A.7
  • 17
    • 0028231924 scopus 로고
    • Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity
    • D.D. Pittman, K.N. Tomkinson, D. Michnick, U. Selighsohn, and R.J. Kaufman Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity Biochemistry 33 1994 6952 6959
    • (1994) Biochemistry , vol.33 , pp. 6952-6959
    • Pittman, D.D.1    Tomkinson, K.N.2    Michnick, D.3    Selighsohn, U.4    Kaufman, R.J.5
  • 18
    • 0028058606 scopus 로고
    • Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage
    • D.A. Michnick, D.D. Pittman, R.J. Wise, and R.J. Kaufman Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage J. Biol. Chem. 269 1994 20095 20102
    • (1994) J. Biol. Chem. , vol.269 , pp. 20095-20102
    • Michnick, D.A.1    Pittman, D.D.2    Wise, R.J.3    Kaufman, R.J.4
  • 19
    • 0040182343 scopus 로고
    • Sulfation of tyrosine residues increases activity of the fourth component of complement
    • G.L. Hortin, T.C. Farries, J.P. Graham, and J.P. Atkinson Sulfation of tyrosine residues increases activity of the fourth component of complement Proc. Natl. Acad. Sci. USA 86 1989 1338 1342
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1338-1342
    • Hortin, G.L.1    Farries, T.C.2    Graham, J.P.3    Atkinson, J.P.4
  • 20
    • 0037189547 scopus 로고    scopus 로고
    • Reduced body weight and increased postimplantation fetal death in tyrosylprotein sulfotransferase-1-deficient mice
    • Y.B. Ouyang, J.T. Crawley, C.E. Aston, and K.L. Moore Reduced body weight and increased postimplantation fetal death in tyrosylprotein sulfotransferase-1-deficient mice J. Biol. Chem. 277 2002 23781 23787
    • (2002) J. Biol. Chem. , vol.277 , pp. 23781-23787
    • Ouyang, Y.B.1    Crawley, J.T.2    Aston, C.E.3    Moore, K.L.4
  • 23
    • 0033621541 scopus 로고    scopus 로고
    • Cuticle collagen genes. Expression in Caenorhabditis elegans
    • I.L. Johnstone Cuticle collagen genes. Expression in Caenorhabditis elegans Trends Genet. 16 2000 21 27
    • (2000) Trends Genet. , vol.16 , pp. 21-27
    • Johnstone, I.L.1
  • 24
    • 0025274443 scopus 로고
    • The Caenorhabditis elegans rol-6 gene, which interacts with the sqt-1 collagen gene to determine organismal morphology, encodes a collagen
    • J.M. Kramer, R.P. French, E.C. Park, and J.J. Johnson The Caenorhabditis elegans rol-6 gene, which interacts with the sqt-1 collagen gene to determine organismal morphology, encodes a collagen Mol. Cell Biol. 10 1990 2081 2089
    • (1990) Mol. Cell Biol. , vol.10 , pp. 2081-2089
    • Kramer, J.M.1    French, R.P.2    Park, E.C.3    Johnson, J.J.4
  • 25
    • 0027442838 scopus 로고
    • Analysis of mutations in the sqt-1 and rol-6 collagen genes of Caenorhabditis elegans
    • J.M. Kramer, and J.J. Johnson Analysis of mutations in the sqt-1 and rol-6 collagen genes of Caenorhabditis elegans Genetics 135 1993 1035 1045
    • (1993) Genetics , vol.135 , pp. 1035-1045
    • Kramer, J.M.1    Johnson, J.J.2
  • 26
    • 0028230454 scopus 로고
    • In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly
    • J. Yang, and J.M. Kramer In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly Mol. Cell Biol. 14 1994 2722 2730
    • (1994) Mol. Cell Biol. , vol.14 , pp. 2722-2730
    • Yang, J.1    Kramer, J.M.2
  • 27
    • 0141535021 scopus 로고    scopus 로고
    • Neuron cell type-specific SNAP-25 expression driven by multiple regulatory elements in the nematode Caenorhabditis elegans
    • S.B. Hwang, and J. Lee Neuron cell type-specific SNAP-25 expression driven by multiple regulatory elements in the nematode Caenorhabditis elegans J. Mol. Biol. 333 2003 237 247
    • (2003) J. Mol. Biol. , vol.333 , pp. 237-247
    • Hwang, S.B.1    Lee, J.2
  • 28
    • 0030820910 scopus 로고    scopus 로고
    • New consensus features for tyrosine O-sulfation determined by mutational analysis
    • J.R. Bundgaard, J. Vuust, and J.F. Rehfeld New consensus features for tyrosine O-sulfation determined by mutational analysis J. Biol. Chem. 272 1997 21700 21705
    • (1997) J. Biol. Chem. , vol.272 , pp. 21700-21705
    • Bundgaard, J.R.1    Vuust, J.2    Rehfeld, J.F.3
  • 29
    • 0036088377 scopus 로고    scopus 로고
    • The Sulfinator: Predicting tyrosine sulfation sites in protein sequences
    • F. Monigatti, E. Gasteiger, A. Bairoch, and E. Jung The Sulfinator: predicting tyrosine sulfation sites in protein sequences Bioinformatics 18 2002 769 770
    • (2002) Bioinformatics , vol.18 , pp. 769-770
    • Monigatti, F.1    Gasteiger, E.2    Bairoch, A.3    Jung, E.4
  • 30
    • 0033512008 scopus 로고    scopus 로고
    • Reevaluation of the determinants of tyrosine sulfation
    • H.B. Nicholas Jr., S.S. Chan, and G.L. Rosenquist Reevaluation of the determinants of tyrosine sulfation Endocrine 11 1999 285 292
    • (1999) Endocrine , vol.11 , pp. 285-292
    • Nicholas Jr., H.B.1    Chan, S.S.2    Rosenquist, G.L.3
  • 31
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • J.M. Souza, B.I. Giasson, Q. Chen, V.M. Lee, and H. Ischiropoulos Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies J. Biol. Chem. 275 2000 18344 18349
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 32
    • 0035921417 scopus 로고    scopus 로고
    • Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox
    • W.A. Edens Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox J. Cell Biol. 154 2001 879 892
    • (2001) J. Cell Biol. , vol.154 , pp. 879-892
    • Edens, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.